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Conserved domains on  [gi|2166948762|ref|XP_045329269|]
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zinc finger protein 674 isoform X4 [Leopardus geoffroyi]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204699)

KRAB (Kruppel-associated box) domain-containing zinc finger protein (KRAB-ZFP) plays important roles in cell differentiation and organ development and in regulating viral replication and transcription; similar to Homo sapiens zinc finger protein 2 that may be involved in transcriptional regulation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-65 8.26e-31

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 114.23  E-value: 8.26e-31
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2166948762    8 LTFRDVFVDFTLEEWRCLDLAQKNLYRDVMLENYSHLVSVGQLVPKPDVVIRLGQGEE 65
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
245-570 1.95e-12

FOG: Zn-finger [General function prediction only];


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 69.34  E-value: 1.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 245 KPYECSECTRAFSQKSTLIAHQRTHTGEKPYECS--ECGKTFIQKSTLMKHTRTHTAEKPFvcgECAKAFKSSYHLTRHE 322
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSD---LNSKSLPLSNSKASSS 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 323 K----THIRQAFYEGVHCGKSGLTYPRTHMGEKPNCNKHGKPSDEKPNPIKHQRSP---IKEKAYECSKCGKSFRGKSHL 395
Cdd:COG5048   109 SlsssSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSnslHPPLPANSLSKDPSSNLSLLI 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 396 svHQRTHTGEKPYECSICGKTFSGKSHLSVHQRTHTGEKPYECRRCGKAF------GEKSTLVVHHRTHTGEKPYKCGEC 469
Cdd:COG5048   189 --SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLP 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 470 GKAFSEKSPLIKHERIHTGER-PYECSNCGKAFSRKSTLIKHQR--IHTGE--KPYECSE--CGKAFSVKSTLIVHHRTH 542
Cdd:COG5048   267 TASSQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLH 346
                         330       340       350
                  ....*....|....*....|....*....|
gi 2166948762 543 TGEKPYEC--RDCGKAFSGKSTLIKHQRSH 570
Cdd:COG5048   347 TSISPAKEklLNSSSKFSPLLNNEPPQSLQ 376
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
219-241 4.51e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 4.51e-03
                          10        20
                  ....*....|....*....|...
gi 2166948762 219 FECSECGKVFIQKANLVVHQRTH 241
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-65 8.26e-31

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 114.23  E-value: 8.26e-31
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2166948762    8 LTFRDVFVDFTLEEWRCLDLAQKNLYRDVMLENYSHLVSVGQLVPKPDVVIRLGQGEE 65
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
7-48 1.55e-23

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 93.30  E-value: 1.55e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2166948762   7 SLTFRDVFVDFTLEEWRCLDLAQKNLYRDVMLENYSHLVSVG 48
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
8-46 1.24e-18

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 79.13  E-value: 1.24e-18
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2166948762   8 LTFRDVFVDFTLEEWRCLDLAQKNLYRDVMLENYSHLVS 46
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
245-570 1.95e-12

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 69.34  E-value: 1.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 245 KPYECSECTRAFSQKSTLIAHQRTHTGEKPYECS--ECGKTFIQKSTLMKHTRTHTAEKPFvcgECAKAFKSSYHLTRHE 322
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSD---LNSKSLPLSNSKASSS 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 323 K----THIRQAFYEGVHCGKSGLTYPRTHMGEKPNCNKHGKPSDEKPNPIKHQRSP---IKEKAYECSKCGKSFRGKSHL 395
Cdd:COG5048   109 SlsssSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSnslHPPLPANSLSKDPSSNLSLLI 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 396 svHQRTHTGEKPYECSICGKTFSGKSHLSVHQRTHTGEKPYECRRCGKAF------GEKSTLVVHHRTHTGEKPYKCGEC 469
Cdd:COG5048   189 --SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLP 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 470 GKAFSEKSPLIKHERIHTGER-PYECSNCGKAFSRKSTLIKHQR--IHTGE--KPYECSE--CGKAFSVKSTLIVHHRTH 542
Cdd:COG5048   267 TASSQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLH 346
                         330       340       350
                  ....*....|....*....|....*....|
gi 2166948762 543 TGEKPYEC--RDCGKAFSGKSTLIKHQRSH 570
Cdd:COG5048   347 TSISPAKEklLNSSSKFSPLLNNEPPQSLQ 376
zf-H2C2_2 pfam13465
Zinc-finger double domain;
507-530 6.35e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.35e-04
                          10        20
                  ....*....|....*....|....
gi 2166948762 507 LIKHQRIHTGEKPYECSECGKAFS 530
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
219-241 4.51e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 4.51e-03
                          10        20
                  ....*....|....*....|...
gi 2166948762 219 FECSECGKVFIQKANLVVHQRTH 241
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-65 8.26e-31

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 114.23  E-value: 8.26e-31
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2166948762    8 LTFRDVFVDFTLEEWRCLDLAQKNLYRDVMLENYSHLVSVGQLVPKPDVVIRLGQGEE 65
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEE 58
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
7-48 1.55e-23

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 93.30  E-value: 1.55e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2166948762   7 SLTFRDVFVDFTLEEWRCLDLAQKNLYRDVMLENYSHLVSVG 48
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
8-46 1.24e-18

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 79.13  E-value: 1.24e-18
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2166948762   8 LTFRDVFVDFTLEEWRCLDLAQKNLYRDVMLENYSHLVS 46
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
245-570 1.95e-12

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 69.34  E-value: 1.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 245 KPYECSECTRAFSQKSTLIAHQRTHTGEKPYECS--ECGKTFIQKSTLMKHTRTHTAEKPFvcgECAKAFKSSYHLTRHE 322
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSD---LNSKSLPLSNSKASSS 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 323 K----THIRQAFYEGVHCGKSGLTYPRTHMGEKPNCNKHGKPSDEKPNPIKHQRSP---IKEKAYECSKCGKSFRGKSHL 395
Cdd:COG5048   109 SlsssSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSnslHPPLPANSLSKDPSSNLSLLI 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 396 svHQRTHTGEKPYECSICGKTFSGKSHLSVHQRTHTGEKPYECRRCGKAF------GEKSTLVVHHRTHTGEKPYKCGEC 469
Cdd:COG5048   189 --SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSpksllsQSPSSLSSSDSSSSASESPRSSLP 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 470 GKAFSEKSPLIKHERIHTGER-PYECSNCGKAFSRKSTLIKHQR--IHTGE--KPYECSE--CGKAFSVKSTLIVHHRTH 542
Cdd:COG5048   267 TASSQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLH 346
                         330       340       350
                  ....*....|....*....|....*....|
gi 2166948762 543 TGEKPYEC--RDCGKAFSGKSTLIKHQRSH 570
Cdd:COG5048   347 TSISPAKEklLNSSSKFSPLLNNEPPQSLQ 376
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
217-576 2.63e-12

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 68.95  E-value: 2.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 217 KLFECSECGKVFIQKANLVVHQRTHTGEKPYECSECTRAFSQKST--LIAHQRTHTGEKPYECSECGKTFIQKSTLMKHT 294
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 295 RTHTA----EKPFVCGECAKAFKSSYHLTRHEKTHIRQAFYEGVHCGKSGLTYPRTHMGEKPNCNKHGKPSDEKPNPikH 370
Cdd:COG5048   112 SSSSNsndnNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLI--S 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 371 QRSPIKEKAYECSKCGKSFRGKSHLSVHQRTHTGEKPYECSICG----KTFSGKSHLSVHQRTHTGEKPYECRRCGKAFG 446
Cdd:COG5048   190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSqlspKSLLSQSPSSLSSSDSSSSASESPRSSLPTAS 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 447 EKSTLVVHH--RTHTG-EKPYKCGECGKAFSEKSPLIKHER--IHTGE--RPYEC--SNCGKAFSRKSTLIKHQRIHTGE 517
Cdd:COG5048   270 SQSSSPNESdsSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSI 349
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2166948762 518 KPYEC--SECGKAFSVKST-----LIVHHRTHTGEKPYEC--RDCGKAFSGKSTLIKHQRSHTGDKTY 576
Cdd:COG5048   350 SPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPY 417
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
342-530 7.44e-08

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.09  E-value: 7.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 342 TYPRTHMGEKPNCNKHGKPSDEK--PNPIKHQRSPIKEKA--YECSKCGKSFRGKSHLSVHQRT--HTGE--KPYEC--S 411
Cdd:COG5048   248 LSSSDSSSSASESPRSSLPTASSqsSSPNESDSSSEKGFSlpIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpyS 327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 412 ICGKTFSGKSHLSVHQRTHTGEKPYEC--RRCGKAFGEKST-----LVVHHRTHTGEKPYKC--GECGKAFSEKSPLIKH 482
Cdd:COG5048   328 LCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLH 407
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2166948762 483 ERIHTGERPYECSN--CGKAFSRKSTLIKHQRIHTGEKPYECSECGKAFS 530
Cdd:COG5048   408 IITHLSFRPYNCKNppCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRR 457
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
245-418 4.89e-05

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 46.23  E-value: 4.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 245 KPYECSECTRAFSQKSTLIAHQRT--HTGE--KPYECSE--CGKTFIQKSTLMKHTRTHTAEKPFVCgecakafkssyhL 318
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKE------------K 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 319 TRHEKTHIRQAFYE---GVHCGKSGLTYPRTHMGEKPNCNKhgkPSDEKPNPIKH--QRSPIKEKAYECSKCGKSFRGKS 393
Cdd:COG5048   356 LLNSSSKFSPLLNNeppQSLQQYKDLKNDKKSETLSNSCIR---NFKRDSNLSLHiiTHLSFRPYNCKNPPCSKSFNRHY 432
                         170       180
                  ....*....|....*....|....*
gi 2166948762 394 HLSVHQRTHTGEKPYECSICGKTFS 418
Cdd:COG5048   433 NLIPHKKIHTNHAPLLCSILKSFRR 457
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
363-438 3.21e-04

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.53  E-value: 3.21e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2166948762 363 EKPNPIKHQRSPIKEKAYECSKCGKSFRGKSHLSVHQRTHTGEKPYECS--ICGKTFSGKSHLSVHQRTHTGEKPYEC 438
Cdd:COG5048    17 SSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLN 94
zf-H2C2_2 pfam13465
Zinc-finger double domain;
507-530 6.35e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.35e-04
                          10        20
                  ....*....|....*....|....
gi 2166948762 507 LIKHQRIHTGEKPYECSECGKAFS 530
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
394-418 7.29e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 7.29e-04
                          10        20
                  ....*....|....*....|....*
gi 2166948762 394 HLSVHQRTHTGEKPYECSICGKTFS 418
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
233-258 7.36e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 7.36e-04
                          10        20
                  ....*....|....*....|....*.
gi 2166948762 233 NLVVHQRTHTGEKPYECSECTRAFSQ 258
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
479-503 1.01e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.01e-03
                          10        20
                  ....*....|....*....|....*
gi 2166948762 479 LIKHERIHTGERPYECSNCGKAFSR 503
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
492-514 1.44e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 1.44e-03
                          10        20
                  ....*....|....*....|...
gi 2166948762 492 YECSNCGKAFSRKSTLIKHQRIH 514
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
265-286 1.46e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.46e-03
                          10        20
                  ....*....|....*....|..
gi 2166948762 265 HQRTHTGEKPYECSECGKTFIQ 286
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
300-403 1.64e-03

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.24  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 300 EKPFVCG--ECAKAFKSSYHLTRHEKthirqafyEGvHCGksgltyPRTHmgekpncnkhgkpsdEKPNPIKHQRSPIKE 377
Cdd:COG5189   347 GKPYKCPveGCNKKYKNQNGLKYHML--------HG-HQN------QKLH---------------ENPSPEKMNIFSAKD 396
                          90       100
                  ....*....|....*....|....*.
gi 2166948762 378 KAYECSKCGKSFRGKSHLSVHqRTHT 403
Cdd:COG5189   397 KPYRCEVCDKRYKNLNGLKYH-RKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
422-445 2.00e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.00e-03
                          10        20
                  ....*....|....*....|....
gi 2166948762 422 HLSVHQRTHTGEKPYECRRCGKAF 445
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
275-297 2.08e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 2.08e-03
                          10        20
                  ....*....|....*....|...
gi 2166948762 275 YECSECGKTFIQKSTLMKHTRTH 297
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
408-430 2.10e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 2.10e-03
                          10        20
                  ....*....|....*....|...
gi 2166948762 408 YECSICGKTFSGKSHLSVHQRTH 430
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
380-402 2.58e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 2.58e-03
                          10        20
                  ....*....|....*....|...
gi 2166948762 380 YECSKCGKSFRGKSHLSVHQRTH 402
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
451-474 2.77e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 2.77e-03
                          10        20
                  ....*....|....*....|....
gi 2166948762 451 LVVHHRTHTGEKPYKCGECGKAFS 474
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
460-543 3.53e-03

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.09  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2166948762 460 GEKPYKCG--ECGKAFSEKSPLiKHERIHtgerpyecSNCGKAFSRKSTLIKHQRIHTGEKPYECSECGKAFSVKSTLiV 537
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGL-KYHMLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGL-K 415

                  ....*.
gi 2166948762 538 HHRTHT 543
Cdd:COG5189   416 YHRKHS 421
zf-H2C2_2 pfam13465
Zinc-finger double domain;
535-558 4.40e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.40e-03
                          10        20
                  ....*....|....*....|....
gi 2166948762 535 LIVHHRTHTGEKPYECRDCGKAFS 558
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
219-241 4.51e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 4.51e-03
                          10        20
                  ....*....|....*....|...
gi 2166948762 219 FECSECGKVFIQKANLVVHQRTH 241
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
548-570 8.87e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 33.81  E-value: 8.87e-03
                          10        20
                  ....*....|....*....|...
gi 2166948762 548 YECRDCGKAFSGKSTLIKHQRSH 570
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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